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Mutational studies reveal lysine 352 on the large subunit is indispensable for catalytic activity of bi-subunit topoisomerase I from Leishmania donovani.

Molecular and biochemical parasitology - 1 May 2009

Ganguly Agneyo, Sengupta Souvik, Bosedasgupta Somdeb, Roy Amit, Majumder Hemanta K

Abstract excerpt

From the vanadate complex crystal structure of Leishmania donovani topoisomerase I, several amino acid residues have been implicated to be involved in the catalytic reaction. Although several predictions and propositions have been made, the exact role of these amino acids has not yet been clearly demonstrated in vitro. Among these residues, lysine 352 and arginine 314 stand as potential candidates for playing the...

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PMID: 19393162
DOI: 10.1016/j.molbiopara.2009.01.002

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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